The role of chordin fragments generated by partial tolloid cleavage in regulating BMP activity

Troilo H, Barrett AL, Wohl AP, Jowitt TA, Collins RF, Bayley CP, Zuk AV, Sengle G, Baldock C

Biochem. Soc. Trans. 2015 Oct;43(5):795-800

PMID: 26517884

Abstract

Chordin-mediated regulation of bone morphogenetic protein (BMP) family growth factors is essential in early embryogenesis and adult homoeostasis. Chordin binds to BMPs through cysteine-rich von Willebrand factor type C (vWC) homology domains and blocks them from interacting with their cell surface receptors. These domains also self-associate and enable chordin to target related proteins to fine-tune BMP regulation. The chordin-BMP inhibitory complex is strengthened by the secreted glycoprotein twisted gastrulation (Tsg); however, inhibition is relieved by cleavage of chordin at two specific sites by tolloid family metalloproteases. As Tsg enhances this cleavage process, it serves a dual role as both promoter and inhibitor of BMP signalling. Recent developments in chordin research suggest that rather than simply being by-products, the cleavage fragments of chordin continue to play a role in BMP regulation. In particular, chordin cleavage at the C-terminus potentiates its anti-BMP activity in a type-specific manner.

  • Upcoming Events

    1. Women in Science and Society with Sarah Millar

      June 19 @ 1:30 pm - 6:00 pm
    2. 9th PhD student and Postdoc Retreat

      August 22 - August 23
    3. 2nd SFB 829 Connector Meeting

      August 31 @ 3:00 pm - 5:30 pm
    4. International Symposium “Molecular Mechanisms regulating Skin Homeostasis”

      November 12 - November 14
    5. 3rd SFB 829 Connector Meeting

      December 7 @ 3:00 pm - 5:30 pm
  • News

© 2017 SFB 829

Durch die weitere Nutzung der Seite stimmst du der Verwendung von Cookies zu. Weitere Informationen

Die Cookie-Einstellungen auf dieser Website sind auf "Cookies zulassen" eingestellt, um das beste Surferlebnis zu ermöglichen. Wenn du diese Website ohne Änderung der Cookie-Einstellungen verwendest oder auf "Akzeptieren" klickst, erklärst du sich damit einverstanden.

Schließen